Homocytotropic Antibody Response in the Rat Infected with the Nematode, Nippostrongylus Brasiliensis

Abstract

Homocytotropic antibodies produced by the rat in response to infection with N. brasiliensis were found to be heat-labile and susceptible to inactivation by 2-mercaptoethanol. On electrophoresis in agar at pH 8.6, H.A. migrated faster than the bulk of γG-, γA- and γM-globulins. The molecular size of H.A. appeared to be somewhat greater than that of 7 S, but smaller than 19 S globulins. On diethylaminoethyl cellulose chromatography, H.A. was eluted with the peak concentration of γA-globulins. H.A. activity was removed from rat antiserum by absorption with rabbit antiserum to rat immunoglobulins. Although available evidence suggests that H.A. constitutes a unique rat immunoglobulin class analogous to human γE, final assignment should be delayed until the characteristics of the heavy polypeptide chains of rat H.A. have been determined.